Information om | Engelska ordet C-TERMINI

Exempel på hur man kan använda C-TERMINI i en mening

• Topology of a transmembrane protein refers to locations of N- and C-termini of membrane-spanning polypeptide chain with respect to the inner or outer sides of the biological membrane occupied by the protein.
• Domain 4 links the heavy and light chains in addition to a disulfide bond between positions close to the N- and C-termini.
• Each hERG subunit consists of 6 transmembrane alpha helices, numbered S1-S6, a pore helix situated between S5 and S6, and cytoplasmically located N- and C-termini.
• The interfaces between subunits contain a number of salt bridges and hydrogen bonds, and the C-terminus of each subunit is involved in oligomerization by interacting with the C-termini and nucleotide-binding domains of the other subunits.
• Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini.
• These domains are, from N- to C-termini, the insulin-like growth factor binding protein (IGFBP) domain, the von Willebrand type C repeats (vWC) domain, the thrombospondin type 1 repeat (TSR) domain, and a C-terminal domain (CT) with a cysteine knot motif.
• Each of the remaining nine 5′ exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini.
• The protein contains two hydrophobic transmembrane domains that help anchoring the molecule on the ER membrane, such that its large luminal domain orients inside the ER lumen and both the N- and C-termini are facing the cytosol.
• Each of the remaining nine 5′ exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini.
• Each of the remaining nine 5′ exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini.
• Sortase A has been widely used as an in vitro tool to post-translationally modify proteins at the N- and C-termini with an appended label.
• Most proteins of the MR family are all of about the same size (250-350 amino acyl residues) and possess seven transmembrane helical spanners with their N-termini on the outside and their C-termini on the inside.
• pneumoniae protein has both its N- and C-termini in the cytoplasm, a large (~ 60 residue) cytoplasmic domain between TMSs 4 and 5, and a large (~ 80 residue) extracytoplasmic loop between TMSs 7 and 8.
• The N-termini are predicted to be in the vacuolar lumen while the C-termini are thought to be in the cytoplasm.
• While most of the human ATL protein structure is conserved between paralogs, the proteins have non-conserved N- and C-termini with the C-termini of ATL1 and ATL2 being autoinhibitory.

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